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- W2000965291 abstract "Spectrin repeats are triple-helical coiled-coil domains found in many proteins that are regularly subjected to mechanical stress. We used atomic force microscopy technique and steered molecular dynamics simulations to study the behavior of a wild-type spectrin repeat and two mutants. The experiments indicate that spectrin repeats can form stable unfolding intermediates when subjected to external forces. In the simulations the unfolding proceeded via a variety of pathways. Stable intermediates were associated to kinking of the central helix close to a proline residue. A mutant stabilizing the central helix showed no intermediates in experiments, in agreement with simulation. Spectrin repeats may thus function as elastic elements, extendable to intermediate states at various lengths." @default.
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- W2000965291 date "2002-08-01" @default.
- W2000965291 modified "2023-10-12" @default.
- W2000965291 title "Pathways and Intermediates in Forced Unfolding of Spectrin Repeats" @default.
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- W2000965291 doi "https://doi.org/10.1016/s0969-2126(02)00808-0" @default.
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